Protein Information

General Information
MoonProt ID135
First appeared in release1.0
Name(s)Ketol-acid reductoisomerase Acetohydroxy-acid reductoisomerase Alpha-keto-beta-hydroxylacyl reductoisomerase Gene Name: ILV5
UniProt IDP06168 (ILV5_YEAST), Reviewed
GO termsGO:0000002 mitochondrial genome maintenance GO:0008652 cellular amino acid biosynthetic process GO:0009082 branched-chain amino acid biosynthetic process GO:0009097 isoleucine biosynthetic process GO:0009099 valine biosynthetic process GO:0055114 oxidation-reduction process GO:0003690 double-stranded DNA binding GO:0004455 ketol-acid reductoisomerase activity GO:0016491 oxidoreductase activity GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor GO:0046872 metal ion binding GO:0050662 coenzyme binding GO:0005739 mitochondrion GO:0042645 mitochondrial nucleoid
Organisms for which functions have been demonstratedSaccharomyces cerevisiae (yeast, fungi)
Sequence length394
Structure Information
Quaternary structure
SCOPNAD(P)-binding Rossmann-fold domains, phosphogluconate dehydrogenase C-terminal domain-like,
TM Helix Predictionno TM helices
DisProt AnnotationNot in DisProt
Predicted Disorder Regions1-36, 367-373, 391-395
Connections to Disease
Function 1
Function descriptionacetohydroxyacid reductoisomerase, enzyme Amino-acid biosynthesis, L-leucine, L-isoleucine and L-valine biosynthesis (R)-2,3-dihydroxy-3-methylbutanoate + NADP+ => (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ => (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH Cofactor
References for functionJM Baterman, PS Perlman, and RA Butow. (2002) Mutational Bisection of the Mitochondrial DNA Stability and Amino Acid Biosynthetic Functions of Ilv5p of Budding Yeast. Genetics. 161, 1043-1052. PMID: 12136009
E.C. number1.1.1.86
Location of functional site(s)
Cellular location of functionmitochondrion
CommentsNADPH Binding: Glu319, His226, Glu311, Asp315, Lys252, Glu492, Glu496, Ser518. R Dumas, V Biou, F Halgand, et al. (2001) Enzymology, Structure, and Dynamics of Acetohydroxy Acid Isomeroreductase. Accou. Of Chem. Res. 34, 399-408. Mg Binding: Asp315, Glu319. NADPH Binding: Gly132, Gly134, Glu136, Glu143, Asp146, Val258, Val259, Gly265, Arg162, Ser165, Ser167. F Halgand, E Dumas, V Biou, et al. (1999) Characterization of the Conformational Changes of Acetohydroxy Acid Isomeroreductase Induced by the Binding of Mg 2+ Ions, NADPH, and a Competitive Inhibitor. Biochemistry. 38, 6025-6034. Mn and ADP binding: Asp315, Glu496, Ser518. K Thomazeau, R Dumas, F Halgand, et al. (2000) Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose. Acta. Cryst. 56, 389-397.
Function 2
Function descriptionmaintain mitochondrial DNA stability enzyme catalytic function not needed for this role
References for functionO Zelenaya-Troitskaya, PS Perlman, and RA Butow. (1995) An enzyme in yeast mitochondria that catalyzes a step in branched-chain amino acid biosynthesis also functions in mitochondria DNA stability. The EMBO Journ. 14, 3268-3276. PMID: 7621838. JM Baterman, PS Perlman, and RA Butow. (2002) Mutational Bisection of the Mitochondrial DNA Stability and Amino Acid Biosynthetic Functions of Ilv5p of Budding Yeast. Genetics. 161, 1043-1052. PMID: 12136009.
E.C. numberN/A
Location of functional site(s)
Cellular location of functionmitochondria